3TY3
Crystal structure of homoisocitrate dehydrogenase from Schizosaccharomyces pombe bound to glycyl-glycyl-glycine
Summary for 3TY3
| Entry DOI | 10.2210/pdb3ty3/pdb |
| Related | 3TY4 |
| Descriptor | Probable homoisocitrate dehydrogenase, glycylglycylglycine, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | b-hydroxyacid oxidative decarboxylase, amino-acid biosynthesis, lysine biosynthesis, oxidoreductase |
| Biological source | Schizosaccharomyces pombe (Fission yeast) |
| Cellular location | Cytoplasm : O14104 |
| Total number of polymer chains | 2 |
| Total formula weight | 80031.64 |
| Authors | Bulfer, S.L.,Hendershot, J.M.,Trievel, R.C. (deposition date: 2011-09-23, release date: 2011-11-09, Last modification date: 2023-09-13) |
| Primary citation | Bulfer, S.L.,Hendershot, J.M.,Trievel, R.C. Crystal structure of homoisocitrate dehydrogenase from Schizosaccharomyces pombe. Proteins, 80:661-666, 2012 Cited by PubMed Abstract: Homoisocitrate dehydrogenase (HICDH) catalyzes the conversion of homoisocitrate to 2-oxoadipate, the third enzymatic step in the α-aminoadipate pathway by which lysine is synthesized in fungi and certain archaebacteria. This enzyme represents a potential target for anti-fungal drug design. Here, we describe the first crystal structures of a fungal HICDH, including structures of an apoenzyme and a binary complex with a glycine tri-peptide. The structures illustrate the homology of HICDH with other β-hydroxyacid oxidative decarboxylases and reveal key differences with the active site of Thermus thermophilus HICDH that provide insights into the differences in substrate specificity of these enzymes. PubMed: 22105743DOI: 10.1002/prot.23231 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.85 Å) |
Structure validation
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